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Description:
LexA repressor (EC 3.4.21.88).
Molecular weight: 22305
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
07-MAR-2006, entry version 9.
Phylogenetic order:
Bacteria Proteobacteria Gammaproteobacteria Enterobacteriales Enterobacteriaceae Salmonella.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein LEXA_SALTI:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | AL627282 | CAD09221.1 | - |
| EMBL | AE014613 | AAO71607.1 | - |
| HSSP | P03033 | 1JHH | |
| SMR | P0A274 | 2-198.1 | |
| MEROPS | S24.001 | -. | |
| GenomeReviews | AL513382_GR | STY4433.1 | |
| GenomeReviews | AE014613_GR | t4143.1 | |
| HAMAP | MF_00015 | - | 1. |
| InterPro | IPR006199 | LexA_DNA_bd. | |
| InterPro | IPR006200 | Pept_S24_LexA. | |
| InterPro | IPR006198 | Pept_S24_S26. | |
| InterPro | IPR006197 | Pept_S24_SOS. | |
| InterPro | IPR011991 | Wing_hlx_DNA_bd. | |
| Pfam | PF01726 | LexA_DNA_bind | 1. |
| Pfam | PF00717 | Peptidase_S24 | 1. |
| PRINTS | PR00726 | LEXASERPTASE. | |
| TIGRFAMs | TIGR00498 | lexA | 1. |
Keywords:
Autocatalytic cleavage; Complete proteome; DNA damage; DNA repair; DNA replication; DNA-binding; Hydrolase; Repressor; SOS response; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX MEDLINE=21534947; PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P.,
RA Cronin A., Davis P., Davies R.M., Dowd L., White N., Farrar J.,
RA Feltwell T., Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K.,
RA Krogh A., Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C.,
RA Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K.,
RA Whitehead S., Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella
RT enterica serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ty2 / ATCC 700931;
RX MEDLINE=22531367; PubMed=12644504;
RX DOI=10.1128/JB.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J.,
RA Burland V., Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2
RT and CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
Feature:
CHAIN 1 202 LexA repressor.
/FTId=PRO_0000170082.
DNA_BIND 28 48 H-T-H motif (By similarity).
ACT_SITE 119 119 Involved in auto-cleavage (By
similarity).
ACT_SITE 156 156 Involved in auto-cleavage (By
similarity).
SITE 84 85 Cleavage (auto-).
Comments:
-!- FUNCTION: Represses a number of genes involved in the response to
DNA damage (SOS response), including recA and lexA. Binds to the
16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence
of single-stranded DNA, recA interacts with lexA causing an
autocatalytic cleavage which disrupts the DNA-binding part of
lexA, leading to derepression of the SOS regulon and eventually
DNA repair (By similarity).
-!- CATALYTIC ACTIVITY: Hydrolysis of Ala-|-Gly bond in repressor
lexA.
-!- SUBUNIT: Homodimer (By similarity).
-!- SIMILARITY: Belongs to the peptidase S24 family.
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Sequence length: 202
MKALTARQQE VFDLIRDHIS QTGMPPTRAE IAQRLGFRSP NAAEEHLKAL ARKGVLEIVS
GASRGIRLLQ EEEDGLPLVG RVAAGEPLLA QQHIEGHYQV DPSLFKPSAD FLLRVSGMSM
KDIGIMDGDL LAVHKTQDVR NGQVVVARID DEVTVKRLKK QGNKVELLPE NSEFTPIVVD
LREQSFTIEG LAVGVIRNGE WL